ID H3AL63_LATCH Unreviewed; 754 AA.
AC H3AL63;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Methylmalonyl-CoA mutase, mitochondrial {ECO:0000256|ARBA:ARBA00014305};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
DE AltName: Full=Methylmalonyl-CoA isomerase {ECO:0000256|ARBA:ARBA00033108};
GN Name=MMUT {ECO:0000313|Ensembl:ENSLACP00000010384.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000010384.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000010384.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reversible isomerization of methylmalonyl-CoA
CC (MMCoA) (generated from branched-chain amino acid metabolism and
CC degradation of dietary odd chain fatty acids and cholesterol) to
CC succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the
CC tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00023743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2;
CC Evidence={ECO:0000256|ARBA:ARBA00023703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22889;
CC Evidence={ECO:0000256|ARBA:ARBA00023703};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFYH01115831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01115832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01115833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01115834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01115835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01115836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01115837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006000985.1; XM_006000923.1.
DR AlphaFoldDB; H3AL63; -.
DR STRING; 7897.ENSLACP00000010384; -.
DR Ensembl; ENSLACT00000010463.2; ENSLACP00000010384.2; ENSLACG00000009146.2.
DR GeneID; 102348247; -.
DR KEGG; lcm:102348247; -.
DR CTD; 4594; -.
DR eggNOG; ENOG502QQ7X; Eukaryota.
DR GeneTree; ENSGT00390000011892; -.
DR HOGENOM; CLU_009523_3_1_1; -.
DR InParanoid; H3AL63; -.
DR OMA; IQEETHI; -.
DR OrthoDB; 304517at2759; -.
DR TreeFam; TF313557; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009146; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProt.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR CDD; cd03679; MM_CoA_mutase_alpha_like; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR PANTHER; PTHR48101:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 618..750
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 754 AA; 83818 MW; 753DBAEE22A964F6 CRC64;
MLRARRVWSV LTANLVKAPF RPQSSEFNCS FFQTVRSLHR EPLHPEWVAL AKKQLKGKDP
EELIWHTPEG ISIKPLYTKR DTEDLLEELP GVNPYTRGPY PTMYTYRPWT IRQYAGFSTV
EESNKFYRDN IKAGQQGLSV AFDLATHRGY DSDNPRVYGD VGMAGVAIDT VEDTKMLFDG
IPLERMSVSM TMNGAVIPVL AMFIVTGEEQ GVPQNKLTGT IQNDILKEFM VRNTYIFPPE
PSMRVIADIF QYTSQHMPKF NSISISGYHM QEAGANAVLE LAYTVADGLE YCRTGIKAGL
DIDEFAPRLS FFWGIGMNFY MEVAKMRAGR RLWAQLIQEK FKPKNSKSLL LRAHCQTSGW
SLTEQDPYNN IIRTAIEAMA AVFGGTQSLH TNSFDEALGL PTVKSARIAR NTQIIIQEES
GIPKVADPWG GSFMMESLTN EIYDAALKLI NEIEEMGGMA RAVAEGIPKL RIEECAARRQ
ARIDSSAEVI VGVNKYQLEK EETVEVLAID NSLVRNKQIE KLKKVKESRN QEKVDQCLAA
ITECAQTGKG NILELAVAAA RVRCTVGEIT DSMKAVFGEH KASDRMVSGA YRQEFGESDE
IGAALNRVQK FVNCEGRRPR LLVAKMGQDG HDRGAKVIAT GFADLGFDVD IGPLFQTPRE
VAQQAVDADV HCVGVSTLAA GHKTLVPELI KELCSLGRPD ILVICGGVIP PQDYQFLYES
GVSSIFGPGT RITMAAVQVL DDIEKNLEKR QQSM
//
